5T2S: PDB entry 5T2S

Structure of the FHA1 domain of Rad53 bound simultaneously to the BRCT domain of Dbf4 and a phosphopeptide. Determined by X-ray diffraction at 2.4 Å resolution. Released 12 Oct 2016.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 4,285
Mol. weight: 64.85 kDa
Released: 12 Oct 2016

Explore 5T2S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5T2S contains 19 α-helices and 31 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	106-122	17
β-strand	125-128	4	1
α-helix	138-157	20
β-strand	161-163	3	1
β-strand	172-174	3	1
α-helix	182-184	3
α-helix	190-196	7
β-strand	200-202	3	1
α-helix	204-213	10
β-strand	234-241	8	2
β-strand	249-253	5	2
α-helix	255-260	6
β-strand	267-272	6	3
β-strand	279-280	2	3
β-strand	292-296	5	3
β-strand	302-306	5	3
β-strand	313-314	2	2
β-strand	317-318	2	2
α-helix	319-320	2
β-strand	321	1	3
β-strand	325-326	2	3
β-strand	331-335	5	2
β-strand	344-350	7	2
α-helix	352-360	9

Chains B and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3

Chain C: 9 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	106-122	17
β-strand	125-128	4	4
α-helix	138-157	20
α-helix	160	1
β-strand	161-163	3	4
β-strand	172-175	4	4
α-helix	182-184	3
α-helix	190-196	7
β-strand	200-203	4	4
α-helix	204-213	10
β-strand	234-241	8	5
β-strand	249-253	5	5
α-helix	255-260	6
β-strand	265-272	8	6
β-strand	279-280	2	6
β-strand	292-297	6	6
β-strand	302-306	5	6
β-strand	312-314	3	5
β-strand	317-318	2	5
α-helix	319-320	2
β-strand	325-326	2	6
β-strand	331-335	5	5
β-strand	344-350	7	5
α-helix	352-357	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DDK kinase regulatory subunit DBF4,Serine/threonine-protein kinase RAD53	A, C	protein	264	Saccharomyces cerevisiae	P22216 (AlphaFold model), P32325 (AlphaFold model)
Asp-gly-glu-ser-tpo-asp-glu-asp-asp	B, D	protein	12	Saccharomyces cerevisiae	P06243 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>5T2S_1 DDK kinase regulatory subunit DBF4,Serine/threonine-protein kinase RAD53 (chains A, C)
SHMTPKELLEWQTNWKKIMKRDSRIYFDITDDVEMNTYNKSKMDKRRDLLKRGFLTLGAQ
ITQFFDTTVTIVITRRSVENIYLLKDTDILSRAKKNYMKVWSYEKAARFLKNLDVDLDHV
DGSKFSQEQIGENIVCRVICTTGQIPIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHL
GNISRLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVES
DILSLVIFINDKFKQCLEQNKVDR

Sequence of entity 2 (B, D), FASTA

>5T2S_2 ASP-GLY-GLU-SER-TPO-ASP-GLU-ASP-ASP (chains B, D)
DGESTDEDDVVS

Primary citation

'AND' logic gates at work: Crystal structure of Rad53 bound to Dbf4 and Cdc7. Almawi, A.W., Matthews, L.A., Myrox, P. et al. Sci Rep (2016) 6:34237-34237. DOI 10.1038/srep34237 · PubMed

Other PDB entries of the same protein (UniProt P22216 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1G6G 1.6 Å, X-ray structure of the N-terminal fha domain from S. Cerevisiae RAD53P in complex with a…
4PDP 2.59 Å, Crystal structure of Rad53 kinase domain and SCD2
6C4U 2.6 Å, Engineered FHA with Myc-pTBD peptide
5T2F 2.66 Å, Structure of the FHA1 domain of Rad53 bound to the BRCT domain of Dbf4
5XZW 2.8 Å, Crystal structure of Rad53 1-466
4PDS 2.9 Å, Crystal structure of Rad53 kinase domain and SCD2 in complex with AMPPNP
2YGV 2.94 Å, Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the…
5XZV 3.1 Å, Crystal structure of Rad53 1-466 in complex with AMP-PNP
1DMZ A refined NMR structure of a new phophopeptide-binding domain containing the FHA2 of RAD53
1FHQ Refined solution structure of the FHA2 domain of RAD53
1FHR Solution structure of the FHA2 domain of RAD53 complexed with a phosphotyrosyl peptide
1G3G NMR structure of the FHA1 domain of yeast RAD53

Browse structure collections

About this viewer

MolViewer shows 5T2S directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.